title: Protein modeling of human prorenin using the molecular dynamics method.
abstract: To study the activation-inactivation mechanism of the renin zymogen, prorenin, a tertiary structural model of human prorenin was constructed using computer graphics and molecular dynamics calculations, based on the pepsinogen structure. This prorenin model shows that the folded prosegment polypeptide can fit into the substrate binding cleft of the renin moiety. The three positively charged residues, Arg10, Arg15, and Arg20, in the prosegment make salt bridges with Asp225, Glu331, and Asp60, respectively, in renin. Arg43, which is in the processing site, forms salt bridges with the catalytic residues of Asp81 and Asp269. These ionic interactions between the prosegment and the renin may contribute to keeping the prorenin structure as an inactive form.
authors.affiliation: Protein Engineering Research Institute, Osaka, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Shiratori
authors.forename: S
authors.initials: S
authors.lastname: Nakagawa
authors.forename: H
authors.initials: H
authors.lastname: Hori
authors.forename: K
authors.initials: K
authors.lastname: Murakami
authors.forename: H
authors.initials: H
authors.lastname: Umeyama
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003196:Computer Graphics; D004792:Enzyme Precursors / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010435:Pepsinogens / Q000737:chemistry; D012083:Renin / Q000737:chemistry*; D016415:Sequence Alignment
chemical_list: D004792:Enzyme Precursors; D010435:Pepsinogens; D012083:Renin